A preliminary evaluation of the differences in the glycosylation of alpha-1-acid glycoprotein between individual liver diseases

被引:37
作者
Anderson, N
Pollacchi, A
Hayes, P
Therapondos, G
Newsome, P
Boyter, A
Smith, K [1 ]
机构
[1] Univ Strathclyde, Glasgow G1 1XW, Lanark, Scotland
[2] Royal Infirm, Liver Unit, Edinburgh, Midlothian, Scotland
关键词
D O I
10.1002/bmc.167
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
During the acute phase response (APR) to tissue injury or infection, the liver is responsible for the level of mediators such as cytokines required at the site of inflammation and providing the essential components for wound healing and tissue repair. Additionally there are substantial alterations in the expression of plasma proteins of hepatic origin such as alpha-1-acid glycoprotein (AGP). The APR also results in alterations to the branching, sialylation and fucosylation of the oligosaccharide chains of AGP. This study investigated whether liver damage could be correlated with changes in AGP glycosylation in groups of patients with various liver diseases (alcoholic liver disease, hepatitis B, hepatitis C, cirrhosis). Hyperfucosylation occurred in all cases of liver disease, although the hepatitis B and C samples showed a more significant increase in comparison with the others. Additionally N-acetylgalactosamine (GalNAc) was detected in the majority of the hepatitis C samples, which was unexpected since this monosaccharide is not a usual component of the N-linked oligosaccharide chains. It was also determined by concanavalin (con) A chromatography that there is a shift towards the increased branching of the oligosaccharide chains in inflammatory liver diseases compared to normal serum. Copyright (C) 2002 John Wiley Sons, Ltd.
引用
收藏
页码:365 / 372
页数:8
相关论文
共 16 条
[1]  
CLEMENTSON KJ, 1997, GLYCOPROTEINS, V2, P173
[2]   INFLAMMATION-INDUCED EXPRESSION OF SIALYL LEWIS X-CONTAINING GLYCAN STRUCTURES ON ALPHA-1-ACID GLYCOPROTEIN (OROSOMUCOID) IN HUMAN SERA [J].
DEGRAAF, TW ;
VANDERSTELT, ME ;
ANBERGEN, MG ;
VANDIJK, W .
JOURNAL OF EXPERIMENTAL MEDICINE, 1993, 177 (03) :657-666
[3]   Investigation into the Concanavalin A reactivity, fucosylation and oligosaccharide microheterogeneity of alpha(1)-acid glycoprotein expressed in the sera of patients with rheumatoid arthritis [J].
Elliott, MA ;
Elliott, HG ;
Gallagher, K ;
McGuire, J ;
Field, M ;
Smith, KD .
JOURNAL OF CHROMATOGRAPHY B, 1997, 688 (02) :229-237
[4]   MICROHETEROGENEITY OF ALPHA-1 ACID GLYCOPROTEIN IN RHEUMATOID-ARTHRITIS - DEPENDENT ON DISEASE DURATION [J].
HRYCAJ, P ;
SOBIESKA, M ;
MACKIEWICZ, S ;
MULLER, W .
ANNALS OF THE RHEUMATIC DISEASES, 1993, 52 (02) :138-141
[5]  
Jorgensen HG, 1998, BIOMED CHROMATOGR, V12, P343, DOI 10.1002/(SICI)1099-0801(199811/12)12:6<343::AID-BMC760>3.0.CO
[6]  
2-6
[7]  
KREMER JMH, 1988, PHARMACOL REV, V40, P1
[8]   Diagnosis of hepatitis C [J].
Lok, ASF ;
Gunaratnam, NT .
HEPATOLOGY, 1997, 26 (03) :S48-S56
[9]   FRACTIONATION OF GLYCOPEPTIDES BY AFFINITY COLUMN CHROMATOGRAPHY ON CONCANAVALIN A-SEPHAROSE [J].
OGATA, S ;
MURAMATSU, T ;
KOBATA, A .
JOURNAL OF BIOCHEMISTRY, 1975, 78 (04) :687-696
[10]   CON A-NONREACTIVE HUMAN ALPHA-1-ACID GLYCOPROTEIN (AGP) IS MORE EFFECTIVE IN MODULATION OF LYMPHOCYTE-PROLIFERATION THAN CON A-REACTIVE AGP SERUM VARIANTS [J].
POS, O ;
OOSTENDORP, RAJ ;
VANDERSTELT, ME ;
SCHEPER, RJ ;
VANDIJK, W .
INFLAMMATION, 1990, 14 (02) :133-141